Exam 1 - BIO 200 – UW with 100%
Correct Answers
DNA - ANS-Deoxyribonucleic Acid; has H instead of OH- group on 2' of the 6-carbon
ring; its double-helix structure allows the hydrophobic nitrogenous bases to face away
from water, and the bases themselves hydrogen bond to each other. DNA is uber stable
RNA - ANS-
nucleotide - ANS-nucleic acid monomer, comprised of a phosphate group on 5' end and
nitrogenous base on 1' end of carbon ring
nucleic acid - ANS-
phosphodiester linkage - ANS-when the phosphate group on one nucleotide reacts with
the hydroxyl group on another one. this creates a bond with a phosphorus and two ester
(diester) bonds! funny how that works. (ester means an oxygen bonded to two other
groups)
antiparallel - ANS-the DNA chains run in opposite directions (one side going 5'-3' and
the other, 3'-5')
3' - ANS-the end of a chain with the hydroxyl group (carbon #6); this is the growing end
5' - ANS-the end of a chain with the phosphate group (carbon #5) Conventionally, it's
written as 5'-3' (DNA/RNA is also synthesized in the direction); this is the terminal end
complementary base-pairs - ANS-Guanine goes with Cytosine, and Adenine with
thymine. These bases hydrogen bone with each other at the exact right distance (e.g.
two purines would overlap).
central dogma of molecular biology - ANS-DNA--(transcribed into)-->RNA---(translated
to)--->proteins
RNA v. DNA stability - ANS-RNA has an second, relatively-highly-reactive OH-group
AMINO ACIDS - ANS-
chemical evolution - ANS-monomers in the prebiotic soup polymerized to form larger
and more complex molecules, such as the proteins and other types of macromole- cules
found in organisms. This is a difficult step, because mono- mers such as amino acids do
not spontaneously self-assemble into macromolecules such as proteins.
, amino groups/amines - ANS-acts as a base
carboxyl groups - ANS-eg. carboxylic acids
carbonyl groups - ANS-aldehydes especially react to produce larger molecules; has
C=O bond
hydroxyl - ANS-(OH group), highly polar, soluble in water, weak acid
phosphate - ANS-linked together, these store a lot of potential energy due to the
electrons on the phosphate groups crowding (electron repulsion)
sulfhydryl - ANS-thiols; when present in proteins, can form S-S bonds to form proteins
PROTEINS AND ENZYMES - ANS-
macromolecule - ANS-a very large molecule made up of smaller molecules joined
together (aka polymers)
Why R-groups are important - ANS-They enable tertiary structure - R group interactions
cause further folding (after secondary structures have formed) and contribute to the
overall globular protein shape. Also they are what make each amino acid different
molecular chaperones - ANS-proteins that facilitate folding in cells- part of the heat-
shock proteins
heat-shock proteins - ANS-produced after cells experience high temperatures/anything
that undos tertiary structure. they bind to hydrophobic patches that otherwise wouldn't
be exposed; allows proteins to re-fold
saturation kinetics - ANS-even with increased substrate amounts, active sites of
enzymes can only take a certain maximum of substrates in a reaction at the fastest rate
that they can
cofactors - ANS-inorganic ions that interact with enzymes
coenzymes - ANS-organic molecules that reversibly interact with enzymes, such as
electron carriers NADH or FADH2
prosthetic groups - ANS-non-amino acid atoms/molecules that are permenantly
attached to proteins
induced fit - ANS-change in chape of an enzyme that occurs when a substrate binds to
the active site.
Correct Answers
DNA - ANS-Deoxyribonucleic Acid; has H instead of OH- group on 2' of the 6-carbon
ring; its double-helix structure allows the hydrophobic nitrogenous bases to face away
from water, and the bases themselves hydrogen bond to each other. DNA is uber stable
RNA - ANS-
nucleotide - ANS-nucleic acid monomer, comprised of a phosphate group on 5' end and
nitrogenous base on 1' end of carbon ring
nucleic acid - ANS-
phosphodiester linkage - ANS-when the phosphate group on one nucleotide reacts with
the hydroxyl group on another one. this creates a bond with a phosphorus and two ester
(diester) bonds! funny how that works. (ester means an oxygen bonded to two other
groups)
antiparallel - ANS-the DNA chains run in opposite directions (one side going 5'-3' and
the other, 3'-5')
3' - ANS-the end of a chain with the hydroxyl group (carbon #6); this is the growing end
5' - ANS-the end of a chain with the phosphate group (carbon #5) Conventionally, it's
written as 5'-3' (DNA/RNA is also synthesized in the direction); this is the terminal end
complementary base-pairs - ANS-Guanine goes with Cytosine, and Adenine with
thymine. These bases hydrogen bone with each other at the exact right distance (e.g.
two purines would overlap).
central dogma of molecular biology - ANS-DNA--(transcribed into)-->RNA---(translated
to)--->proteins
RNA v. DNA stability - ANS-RNA has an second, relatively-highly-reactive OH-group
AMINO ACIDS - ANS-
chemical evolution - ANS-monomers in the prebiotic soup polymerized to form larger
and more complex molecules, such as the proteins and other types of macromole- cules
found in organisms. This is a difficult step, because mono- mers such as amino acids do
not spontaneously self-assemble into macromolecules such as proteins.
, amino groups/amines - ANS-acts as a base
carboxyl groups - ANS-eg. carboxylic acids
carbonyl groups - ANS-aldehydes especially react to produce larger molecules; has
C=O bond
hydroxyl - ANS-(OH group), highly polar, soluble in water, weak acid
phosphate - ANS-linked together, these store a lot of potential energy due to the
electrons on the phosphate groups crowding (electron repulsion)
sulfhydryl - ANS-thiols; when present in proteins, can form S-S bonds to form proteins
PROTEINS AND ENZYMES - ANS-
macromolecule - ANS-a very large molecule made up of smaller molecules joined
together (aka polymers)
Why R-groups are important - ANS-They enable tertiary structure - R group interactions
cause further folding (after secondary structures have formed) and contribute to the
overall globular protein shape. Also they are what make each amino acid different
molecular chaperones - ANS-proteins that facilitate folding in cells- part of the heat-
shock proteins
heat-shock proteins - ANS-produced after cells experience high temperatures/anything
that undos tertiary structure. they bind to hydrophobic patches that otherwise wouldn't
be exposed; allows proteins to re-fold
saturation kinetics - ANS-even with increased substrate amounts, active sites of
enzymes can only take a certain maximum of substrates in a reaction at the fastest rate
that they can
cofactors - ANS-inorganic ions that interact with enzymes
coenzymes - ANS-organic molecules that reversibly interact with enzymes, such as
electron carriers NADH or FADH2
prosthetic groups - ANS-non-amino acid atoms/molecules that are permenantly
attached to proteins
induced fit - ANS-change in chape of an enzyme that occurs when a substrate binds to
the active site.
